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Database: UniProt
Entry: S7VCJ3_9BACT
LinkDB: S7VCJ3_9BACT
Original site: S7VCJ3_9BACT 
ID   S7VCJ3_9BACT            Unreviewed;       352 AA.
AC   S7VCJ3;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Cytochrome c551 peroxidase {ECO:0000313|EMBL:EPR67975.1};
DE            EC=1.11.1.5 {ECO:0000313|EMBL:EPR67975.1};
GN   ORFNames=ADICYQ_3047 {ECO:0000313|EMBL:EPR67975.1};
OS   Cyclobacterium qasimii M12-11B.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Cyclobacterium.
OX   NCBI_TaxID=641524 {ECO:0000313|EMBL:EPR67975.1, ECO:0000313|Proteomes:UP000014974};
RN   [1] {ECO:0000313|EMBL:EPR67975.1, ECO:0000313|Proteomes:UP000014974}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M12-11B {ECO:0000313|EMBL:EPR67975.1,
RC   ECO:0000313|Proteomes:UP000014974};
RX   PubMed=23950138;
RA   Shivaji S., Ara S., Singh A., Kumar Pinnaka A.;
RT   "Draft Genome Sequence of Cyclobacterium qasimii Strain M12-11BT, Isolated
RT   from Arctic Marine Sediment.";
RL   Genome Announc. 1:e00642-13(2013).
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000294-1};
CC       Note=Binds 2 heme groups. {ECO:0000256|PIRSR:PIRSR000294-1};
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC   -!- PTM: Binds 2 heme groups per subunit. {ECO:0000256|PIRSR:PIRSR000294-
CC       1}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EPR67975.1}.
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DR   EMBL; ATNM01000110; EPR67975.1; -; Genomic_DNA.
DR   RefSeq; WP_020888909.1; NZ_ATNM01000110.1.
DR   AlphaFoldDB; S7VCJ3; -.
DR   STRING; 641524.ADICYQ_3047; -.
DR   eggNOG; COG1858; Bacteria.
DR   OrthoDB; 9805202at2; -.
DR   Proteomes; UP000014974; Unassembled WGS sequence.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004130; F:cytochrome-c peroxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.760.10; Cytochrome c-like domain; 2.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR004852; Di-haem_cyt_c_peroxidsae.
DR   InterPro; IPR026259; MauG/Cytc_peroxidase.
DR   PANTHER; PTHR30600; CYTOCHROME C PEROXIDASE-RELATED; 1.
DR   Pfam; PF03150; CCP_MauG; 1.
DR   PIRSF; PIRSF000294; Cytochrome-c_peroxidase; 1.
DR   SUPFAM; SSF46626; Cytochrome c; 2.
DR   PROSITE; PS51007; CYTC; 1.
PE   4: Predicted;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR000294-1};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000294-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000294-2};
KW   Oxidoreductase {ECO:0000313|EMBL:EPR67975.1};
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW   Peroxidase {ECO:0000313|EMBL:EPR67975.1};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..352
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004558265"
FT   DOMAIN          212..340
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   BINDING         82
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000294-1"
FT   BINDING         85
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000294-1"
FT   BINDING         86
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000294-2"
FT   BINDING         225
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000294-1"
FT   BINDING         228
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000294-1"
FT   BINDING         229
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000294-2"
SQ   SEQUENCE   352 AA;  39280 MW;  7446A66CAAF5C11D CRC64;
     MDCYKISLSF ILLAAGFLNA CLPVNEEIGK ITPEYYVPVY SSSLQQEDFP QPERNYLSKE
     GVELGKILFF DPELSANGKI SCAGCHLPEK AFSDGLALTN IGVSGLALHR NSPALFNLAW
     HDGLFWEGGA NDLESMVFGP LTHPDEMAAD LTEALQYINT HDTYPLLFKE AFPSDSITSA
     AIARSLAQFM RTLISDGSKY DQWIREETAL SSEELKGYEV YKENCSSCHK EGLFTDLSYH
     NNGLDSSYPD PPELEGLYQG RYRITFKDED MGTYKTASLR NLSFTAPYMH DGRFSSLDEV
     LDHYESGIKT NETLAPQLEN GIVLSAAERT QLLAFLNSLN DNNFITNPAY QK
//
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